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Literature summary for 1.4.9.1 extracted from

  • Shin, S.; Abu Tarboush, N.; Davidson, V.L.
    Long-range electron transfer reactions between hemes of MauG and different forms of tryptophan tryptophylquinone of methylamine dehydrogenase (2010), Biochemistry, 49, 5810-5816.
    View publication on PubMedView publication on EuropePMC

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
119000
-
-
Paracoccus denitrificans

Organism

Organism UniProt Comment Textmining
Paracoccus denitrificans
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification the diheme enzymeMauG catalyzes the post-translational modification of a precursor protein of methylamine dehydrogenase, preMADH, to complete the biosynthesis of its protein-derived tryptophan tryptophylquinone, TTQ, cofactor. This six-electron oxidation of preMADH requires long-range electron transfer as the structure of the MauG-preMADH complex reveals that the shortest distance between the modified residues of preMADH and the nearest heme of MauG is 14.0 A. Steady-state kinetic and single turnover kinetic studies of MauG-dependent oxidation of quinol MADH at pH 7.5, 25°C, overview Paracoccus denitrificans

Subunits

Subunits Comment Organism
heterotetramer alpha2beta2 protein, with each beta subunit possessing a tryptophan tryptophylquinone, TTQ, protein-derived cofactor Paracoccus denitrificans

Synonyms

Synonyms Comment Organism
MADH
-
Paracoccus denitrificans
methylamine dehydrogenase
-
Paracoccus denitrificans

Cofactor

Cofactor Comment Organism Structure
tryptophan tryptophylquinone a two-electron redox cofactor, each beta subunit of the heterotetrameric enzyme NADH possesses a tryptophan tryptophylquinone, TTQ, protein-derived cofactor. TTQ is formed by post-translational modification of two tryptophan residues of the preMADH polypeptide chain through the diheme enzyme MauG. This six-electron oxidation of preMADH requires long-range electron transfer as the structure of the MauG-preMADH complex reveals that the shortest distance between the modified residues of preMADH and the nearest heme of MauG is 14.0 A, overview Paracoccus denitrificans

General Information

General Information Comment Organism
additional information steady-state MauG-depedent TTQ biosynthesis using quinol MADH as a substrate and single-turnover kinetics of the reaction of bis-Fe(IV) MauG with quinol MADH, overview Paracoccus denitrificans